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Database: PDB
Entry: 1G23
LinkDB: 1G23
Original site: 1G23 
HEADER    TRANSFERASE                             16-OCT-00   1G23              
TITLE     THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF     
TITLE    2 GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). GLUCOSE-1-PHOSPHATE
TITLE    3 COMPLEX.                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE;                 
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 SYNONYM: GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA);           
COMPND   5 EC: 2.7.7.24;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 287;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(LAMBDA DE3);                          
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET23A(+)                                 
KEYWDS    L-RHAMNOSE, NUCLEOTIDYLTRANSFERASE, PYROPHOSPHORYLASE,                
KEYWDS   2 THYMIDYLYLTRANSFERASE, ALLOSTERY, TRANSFERASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.BLANKENFELDT,M.ASUNCION,J.S.LAM,J.H.NAISMITH                        
REVDAT   4   29-JUL-20 1G23    1       COMPND REMARK SEQADV HETNAM              
REVDAT   4 2                   1       LINK   SITE                              
REVDAT   3   24-FEB-09 1G23    1       VERSN                                    
REVDAT   2   01-APR-03 1G23    1       JRNL                                     
REVDAT   1   27-DEC-00 1G23    0                                                
JRNL        AUTH   W.BLANKENFELDT,M.ASUNCION,J.S.LAM,J.H.NAISMITH               
JRNL        TITL   THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND          
JRNL        TITL 2 REGULATION OF GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE      
JRNL        TITL 3 (RMLA).                                                      
JRNL        REF    EMBO J.                       V.  19  6652 2000              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   11118200                                                     
JRNL        DOI    10.1093/EMBOJ/19.24.6652                                     
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   W.BLANKENFELDT,M.F.GIRAUD,G.LEONARD,R.RAHIM,C.CREUZENET,     
REMARK   1  AUTH 2 J.S.LAM,J.H.NAISMITH                                         
REMARK   1  TITL   THE PURIFICATION, CRYSTALLISATION AND PRELIMINARY STRUCTURAL 
REMARK   1  TITL 2 CHARACTERISATION OF GLUCOSE-1-PHOSPHATE                      
REMARK   1  TITL 3 THYMIDYLYLTRANSFERASE (RMLA), THE FIRST ENZYME OF THE        
REMARK   1  TITL 4 DTDP-L-RHAMNOSE SYNTHESIS PATHWAY FROM PSEUDOMONAS           
REMARK   1  TITL 5 AERUGINOSA                                                   
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  56  1501 2000              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  DOI    10.1107/S0907444900010040                                    
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   A.MELO,L.GLASER                                              
REMARK   1  TITL   THE NUCLEOTIDE SPECIFICITY AND FEEDBACK CONTROL OF THYMIDINE 
REMARK   1  TITL 2 DIPHOSPHATE D-GLUCOSE PYROPHOSPHORYLASE.                     
REMARK   1  REF    J.BIOL.CHEM.                  V. 240   398 1965              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 72.55                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 58982                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3103                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 69.40                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2320                       
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL                         
REMARK   3   BIN FREE R VALUE                    : 0.2870                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 18280                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 193                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 49.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.94                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.26000                                              
REMARK   3    B22 (A**2) : 0.28000                                              
REMARK   3    B33 (A**2) : -0.59000                                             
REMARK   3    B12 (A**2) : 0.02000                                              
REMARK   3    B13 (A**2) : 0.15000                                              
REMARK   3    B23 (A**2) : -0.35000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.508         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.408         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.900        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL                          
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : NULL                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1G23 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-NOV-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000012137.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAR-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.885                              
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL CUT MONOCHROMATOR   
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 121112                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.7                               
REMARK 200  DATA REDUNDANCY                : 1.900                              
REMARK 200  R MERGE                    (I) : 0.02400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 29.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.87                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 69.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.08900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 9.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 9-11 % (W/V) PEG 6000, 0.5 M LI          
REMARK 280  -SULFATE, 0.1 M NA-CITRATE, 4+4 MIKROLITRE + 1 MIKROLITRE 100 MM    
REMARK 280  G1P, PH 4.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TETRAMER BEST DESCRIBED AS A    
REMARK 300 DIMER OF DIMERS.                                                     
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15330 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 43220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -143.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16020 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 43110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -178.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MSE A     1                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     MSE C     1                                                      
REMARK 465     MSE D     1                                                      
REMARK 465     MSE E     1                                                      
REMARK 465     MSE F     1                                                      
REMARK 465     MSE G     1                                                      
REMARK 465     MSE H     1                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NE2  GLN B   180     OE1  GLU E   208              2.17            
REMARK 500   O    PRO D   193     N    GLY D   195              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLU C   208     NE2  GLN G   180     1556     2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A 119   CB    HIS A 119   CG     -0.120                       
REMARK 500    ARG A 194   CB    ARG A 194   CG     -0.229                       
REMARK 500    ARG A 194   CZ    ARG A 194   NH1    -0.161                       
REMARK 500    MSE A 217  SE     MSE A 217   CE     -0.416                       
REMARK 500    ILE B  23   CB    ILE B  23   CG2    -0.215                       
REMARK 500    GLN B  26   CD    GLN B  26   OE1    -0.164                       
REMARK 500    HIS B 119   CB    HIS B 119   CG     -0.123                       
REMARK 500    GLN B 152   CG    GLN B 152   CD     -0.215                       
REMARK 500    GLN B 152   CD    GLN B 152   OE1    -0.254                       
REMARK 500    ARG B 194   CB    ARG B 194   CG     -0.240                       
REMARK 500    ARG B 194   CZ    ARG B 194   NH1    -0.169                       
REMARK 500    MSE B 217  SE     MSE B 217   CE     -0.394                       
REMARK 500    HIS B 229   CE1   HIS B 229   NE2    -0.073                       
REMARK 500    GLN B 237   CB    GLN B 237   CG     -0.185                       
REMARK 500    ILE C  23   CA    ILE C  23   CB     -0.139                       
REMARK 500    GLN C  26   CD    GLN C  26   OE1    -0.180                       
REMARK 500    GLN C  26   CD    GLN C  26   NE2    -0.185                       
REMARK 500    GLN C  65   CD    GLN C  65   OE1    -0.145                       
REMARK 500    GLN C  65   CD    GLN C  65   NE2    -0.181                       
REMARK 500    HIS C 119   CB    HIS C 119   CG     -0.117                       
REMARK 500    ASP C 141   CB    ASP C 141   CG     -0.299                       
REMARK 500    ASP C 141   CG    ASP C 141   OD1    -0.149                       
REMARK 500    ARG C 194   CB    ARG C 194   CG     -0.193                       
REMARK 500    ARG C 194   CZ    ARG C 194   NH1    -0.130                       
REMARK 500    ARG C 194   CZ    ARG C 194   NH2    -0.082                       
REMARK 500    MSE C 217  SE     MSE C 217   CE     -0.455                       
REMARK 500    ILE D  23   CB    ILE D  23   CG2    -0.193                       
REMARK 500    MSE D  44  SE     MSE D  44   CE     -0.381                       
REMARK 500    HIS D 119   CA    HIS D 119   CB     -0.135                       
REMARK 500    HIS D 119   CB    HIS D 119   CG     -0.231                       
REMARK 500    THR D 130   CB    THR D 130   CG2    -0.376                       
REMARK 500    ARG D 194   CB    ARG D 194   CG     -0.423                       
REMARK 500    ARG D 194   NE    ARG D 194   CZ     -0.133                       
REMARK 500    ARG D 194   CZ    ARG D 194   NH1    -0.343                       
REMARK 500    ARG D 194   CZ    ARG D 194   NH2    -0.137                       
REMARK 500    MSE D 217  SE     MSE D 217   CE     -0.470                       
REMARK 500    GLN D 237   CB    GLN D 237   CG     -0.172                       
REMARK 500    HIS E 119   CB    HIS E 119   CG     -0.200                       
REMARK 500    LYS E 190   CB    LYS E 190   CG     -0.373                       
REMARK 500    LYS E 190   CG    LYS E 190   CD     -0.240                       
REMARK 500    LYS E 190   CD    LYS E 190   CE     -0.337                       
REMARK 500    ARG E 194   CB    ARG E 194   CG     -0.414                       
REMARK 500    ARG E 194   NE    ARG E 194   CZ     -0.137                       
REMARK 500    ARG E 194   CZ    ARG E 194   NH1    -0.347                       
REMARK 500    ARG E 194   CZ    ARG E 194   NH2    -0.135                       
REMARK 500    MSE E 217  SE     MSE E 217   CE     -0.395                       
REMARK 500    GLN E 237   CB    GLN E 237   CG     -0.165                       
REMARK 500    GLN E 267   CB    GLN E 267   CG     -0.610                       
REMARK 500    GLN E 267   CG    GLN E 267   CD     -0.323                       
REMARK 500    GLN E 267   CD    GLN E 267   OE1    -0.134                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      88 BOND DEVIATIONS.                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ILE A  23   CB  -  CA  -  C   ANGL. DEV. = -13.4 DEGREES          
REMARK 500    ASP A  86   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG A 128   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP A 141   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG A 194   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG A 194   NE  -  CZ  -  NH2 ANGL. DEV. =   7.8 DEGREES          
REMARK 500    ASP B  32   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP B 141   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP B 188   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG B 194   NE  -  CZ  -  NH2 ANGL. DEV. =   7.7 DEGREES          
REMARK 500    GLY C  11   N   -  CA  -  C   ANGL. DEV. =  15.7 DEGREES          
REMARK 500    ASP C 141   CB  -  CG  -  OD1 ANGL. DEV. = -20.0 DEGREES          
REMARK 500    ASP C 141   CB  -  CG  -  OD2 ANGL. DEV. =  17.4 DEGREES          
REMARK 500    ARG C 194   NE  -  CZ  -  NH2 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ILE D  23   CB  -  CA  -  C   ANGL. DEV. = -12.6 DEGREES          
REMARK 500    HIS D 119   CB  -  CA  -  C   ANGL. DEV. = -17.1 DEGREES          
REMARK 500    HIS D 119   N   -  CA  -  CB  ANGL. DEV. =  14.3 DEGREES          
REMARK 500    HIS D 119   CB  -  CG  -  ND1 ANGL. DEV. =  -8.6 DEGREES          
REMARK 500    THR D 130   OG1 -  CB  -  CG2 ANGL. DEV. = -19.1 DEGREES          
REMARK 500    ASP D 141   CB  -  CG  -  OD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ARG D 194   CB  -  CG  -  CD  ANGL. DEV. =  16.9 DEGREES          
REMARK 500    ARG D 194   CG  -  CD  -  NE  ANGL. DEV. =  27.2 DEGREES          
REMARK 500    ARG D 194   NH1 -  CZ  -  NH2 ANGL. DEV. = -11.0 DEGREES          
REMARK 500    ARG D 194   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ARG D 194   NE  -  CZ  -  NH2 ANGL. DEV. =  14.6 DEGREES          
REMARK 500    HIS E 119   CB  -  CA  -  C   ANGL. DEV. = -12.2 DEGREES          
REMARK 500    HIS E 119   N   -  CA  -  CB  ANGL. DEV. =  12.9 DEGREES          
REMARK 500    ASP E 141   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG E 194   CB  -  CG  -  CD  ANGL. DEV. =  15.9 DEGREES          
REMARK 500    ARG E 194   CG  -  CD  -  NE  ANGL. DEV. =  28.1 DEGREES          
REMARK 500    ARG E 194   NH1 -  CZ  -  NH2 ANGL. DEV. = -10.7 DEGREES          
REMARK 500    ARG E 194   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG E 194   NE  -  CZ  -  NH2 ANGL. DEV. =  14.6 DEGREES          
REMARK 500    ASP E 264   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ILE F  23   CB  -  CA  -  C   ANGL. DEV. = -12.9 DEGREES          
REMARK 500    ASP F  32   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP F  59   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    THR F 130   OG1 -  CB  -  CG2 ANGL. DEV. = -23.4 DEGREES          
REMARK 500    ASP F 141   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    LYS F 155   CA  -  CB  -  CG  ANGL. DEV. =  16.1 DEGREES          
REMARK 500    LYS F 155   CD  -  CE  -  NZ  ANGL. DEV. =  20.9 DEGREES          
REMARK 500    ASP F 184   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG F 194   NE  -  CZ  -  NH2 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ARG G 128   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ASP G 141   CB  -  CG  -  OD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP G 188   CB  -  CG  -  OD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ARG G 194   NE  -  CZ  -  NH2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ILE H  23   CG1 -  CB  -  CG2 ANGL. DEV. = -58.5 DEGREES          
REMARK 500    ILE H  23   CA  -  CB  -  CG1 ANGL. DEV. =  19.1 DEGREES          
REMARK 500    ASP H  32   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      57 ANGLE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A  23      153.18    179.54                                   
REMARK 500    TYR A  31      -82.52     64.25                                   
REMARK 500    ASN A 101       31.62    -99.75                                   
REMARK 500    LYS A 162       59.26     37.76                                   
REMARK 500    ARG A 194       -1.16    -51.67                                   
REMARK 500    THR A 226       51.16   -103.78                                   
REMARK 500    TYR B  31      -84.64     63.52                                   
REMARK 500    ASN B 101       32.74    -95.81                                   
REMARK 500    ARG B 194      -13.22    -43.46                                   
REMARK 500    THR B 226       50.77   -106.88                                   
REMARK 500    SER C  12      103.18    -47.97                                   
REMARK 500    THR C  14      -60.08    -23.98                                   
REMARK 500    ARG C  15      -75.89    -44.89                                   
REMARK 500    LEU C  16       17.64    -54.01                                   
REMARK 500    TYR C  31      -80.61     65.85                                   
REMARK 500    PHE C 118      -33.80    -37.37                                   
REMARK 500    LYS C 162       57.23     39.25                                   
REMARK 500    ARG C 194        7.57    -52.31                                   
REMARK 500    THR C 226       52.66   -102.65                                   
REMARK 500    THR D  14      -63.66    -26.08                                   
REMARK 500    HIS D  17      144.89    -34.63                                   
REMARK 500    TYR D  31      -77.30     68.32                                   
REMARK 500    ASP D 179     -158.71    -94.52                                   
REMARK 500    ARG D 194       -9.40    -41.90                                   
REMARK 500    THR D 226       47.45   -105.73                                   
REMARK 500    SER E  12      -48.77    -16.09                                   
REMARK 500    THR E  14      -51.47    -26.25                                   
REMARK 500    ARG E  15      -64.21    -28.30                                   
REMARK 500    LEU E  16       40.37    -91.37                                   
REMARK 500    THR E  20       20.50    -77.98                                   
REMARK 500    TYR E  31      -78.41     59.74                                   
REMARK 500    PRO E  85       58.93    -59.45                                   
REMARK 500    LYS E 162       53.47     34.87                                   
REMARK 500    ARG E 194       -7.84    -44.37                                   
REMARK 500    THR E 226       49.00   -104.89                                   
REMARK 500    THR F  14      -60.06    -22.10                                   
REMARK 500    TYR F  31      -77.50     64.59                                   
REMARK 500    THR F 226       49.80   -100.52                                   
REMARK 500    TYR G  31      -84.88     66.63                                   
REMARK 500    ARG G 194       -9.37    -48.52                                   
REMARK 500    THR G 226       43.58   -108.89                                   
REMARK 500    LEU H  21      -79.69    -63.82                                   
REMARK 500    TYR H  31      -81.11     65.41                                   
REMARK 500    ASP H 179     -157.13    -86.32                                   
REMARK 500    ARG H 194       -1.28    -52.04                                   
REMARK 500    THR H 226       46.10   -104.31                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    HIS B 119         0.08    SIDE CHAIN                              
REMARK 500    HIS C 119         0.08    SIDE CHAIN                              
REMARK 500    HIS D 119         0.11    SIDE CHAIN                              
REMARK 500    HIS E 119         0.11    SIDE CHAIN                              
REMARK 500    HIS F 116         0.12    SIDE CHAIN                              
REMARK 500    HIS F 119         0.09    SIDE CHAIN                              
REMARK 500    HIS F 229         0.08    SIDE CHAIN                              
REMARK 500    HIS G 116         0.10    SIDE CHAIN                              
REMARK 500    HIS G 119         0.10    SIDE CHAIN                              
REMARK 500    HIS H 119         0.12    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FXO   RELATED DB: PDB                                   
REMARK 900 1FXO IS RMLA IN COMPLEX WITH 2'-DEOXY-THYMIDINE-5'-MONOPHOSPHATE     
REMARK 900 (TMP)                                                                
REMARK 900 RELATED ID: 1FZW   RELATED DB: PDB                                   
REMARK 900 1FZW IS RMLA APO ENZYME                                              
REMARK 900 RELATED ID: 1G0R   RELATED DB: PDB                                   
REMARK 900 1G0R IS RMLA IN COMPLEX WITH 2'-DEOXY-THIMIDINE (THM) AND ALPHA-D-   
REMARK 900 GLUCOSE-1-PHOSPHATE (G1P)                                            
REMARK 900 RELATED ID: 1G1L   RELATED DB: PDB                                   
REMARK 900 1G1L IS RMLA IN COMPLEX WITH 2'-DEOXY-THYMIDINE-ALPHA-D-GLUCOSE      
REMARK 900 (TDG)                                                                
REMARK 900 RELATED ID: 1G2V   RELATED DB: PDB                                   
REMARK 900 1G2V IS RMLA IN COMPLEX WITH 2'-DEOXY-THYMIDINE-5'-TRIPHOSPHATE      
REMARK 900 (TTP)                                                                
REMARK 900 RELATED ID: 1G31   RELATED DB: PDB                                   
REMARK 900 1G31 IS RMLA IN COMPLEX WITH 2'-DEOXY-THYMIDINE-BETA-L-RHAMNOSE      
REMARK 900 (TDR)                                                                
DBREF  1G23 A    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G23 B    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G23 C    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G23 D    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G23 E    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G23 F    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G23 G    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G23 H    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
SEQADV 1G23 MSE A    1  UNP  Q9HU22    MET     1 MODIFIED RESIDUE               
SEQADV 1G23 MSE A   35  UNP  Q9HU22    MET    35 MODIFIED RESIDUE               
SEQADV 1G23 MSE A   44  UNP  Q9HU22    MET    44 MODIFIED RESIDUE               
SEQADV 1G23 MSE A  217  UNP  Q9HU22    MET   217 MODIFIED RESIDUE               
SEQADV 1G23 MSE B    1  UNP  Q9HU22    MET     1 MODIFIED RESIDUE               
SEQADV 1G23 MSE B   35  UNP  Q9HU22    MET    35 MODIFIED RESIDUE               
SEQADV 1G23 MSE B   44  UNP  Q9HU22    MET    44 MODIFIED RESIDUE               
SEQADV 1G23 MSE B  217  UNP  Q9HU22    MET   217 MODIFIED RESIDUE               
SEQADV 1G23 MSE C    1  UNP  Q9HU22    MET     1 MODIFIED RESIDUE               
SEQADV 1G23 MSE C   35  UNP  Q9HU22    MET    35 MODIFIED RESIDUE               
SEQADV 1G23 MSE C   44  UNP  Q9HU22    MET    44 MODIFIED RESIDUE               
SEQADV 1G23 MSE C  217  UNP  Q9HU22    MET   217 MODIFIED RESIDUE               
SEQADV 1G23 MSE D    1  UNP  Q9HU22    MET     1 MODIFIED RESIDUE               
SEQADV 1G23 MSE D   35  UNP  Q9HU22    MET    35 MODIFIED RESIDUE               
SEQADV 1G23 MSE D   44  UNP  Q9HU22    MET    44 MODIFIED RESIDUE               
SEQADV 1G23 MSE D  217  UNP  Q9HU22    MET   217 MODIFIED RESIDUE               
SEQADV 1G23 MSE E    1  UNP  Q9HU22    MET     1 MODIFIED RESIDUE               
SEQADV 1G23 MSE E   35  UNP  Q9HU22    MET    35 MODIFIED RESIDUE               
SEQADV 1G23 MSE E   44  UNP  Q9HU22    MET    44 MODIFIED RESIDUE               
SEQADV 1G23 MSE E  217  UNP  Q9HU22    MET   217 MODIFIED RESIDUE               
SEQADV 1G23 MSE F    1  UNP  Q9HU22    MET     1 MODIFIED RESIDUE               
SEQADV 1G23 MSE F   35  UNP  Q9HU22    MET    35 MODIFIED RESIDUE               
SEQADV 1G23 MSE F   44  UNP  Q9HU22    MET    44 MODIFIED RESIDUE               
SEQADV 1G23 MSE F  217  UNP  Q9HU22    MET   217 MODIFIED RESIDUE               
SEQADV 1G23 MSE G    1  UNP  Q9HU22    MET     1 MODIFIED RESIDUE               
SEQADV 1G23 MSE G   35  UNP  Q9HU22    MET    35 MODIFIED RESIDUE               
SEQADV 1G23 MSE G   44  UNP  Q9HU22    MET    44 MODIFIED RESIDUE               
SEQADV 1G23 MSE G  217  UNP  Q9HU22    MET   217 MODIFIED RESIDUE               
SEQADV 1G23 MSE H    1  UNP  Q9HU22    MET     1 MODIFIED RESIDUE               
SEQADV 1G23 MSE H   35  UNP  Q9HU22    MET    35 MODIFIED RESIDUE               
SEQADV 1G23 MSE H   44  UNP  Q9HU22    MET    44 MODIFIED RESIDUE               
SEQADV 1G23 MSE H  217  UNP  Q9HU22    MET   217 MODIFIED RESIDUE               
SEQRES   1 A  293  MSE LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 A  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 A  293  LEU LEU PRO VAL TYR ASP LYS PRO MSE ILE TYR TYR PRO          
SEQRES   4 A  293  LEU SER THR LEU MSE LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 A  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 A  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 A  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 A  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 A  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 A  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 A  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 A  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 A  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 A  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 A  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 A  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 A  293  ARG GLY GLN LEU SER VAL GLU ILE MSE GLY ARG GLY TYR          
SEQRES  18 A  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 A  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 A  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 A  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 A  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 A  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 B  293  MSE LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 B  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 B  293  LEU LEU PRO VAL TYR ASP LYS PRO MSE ILE TYR TYR PRO          
SEQRES   4 B  293  LEU SER THR LEU MSE LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 B  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 B  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 B  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 B  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 B  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 B  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 B  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 B  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 B  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 B  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 B  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 B  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 B  293  ARG GLY GLN LEU SER VAL GLU ILE MSE GLY ARG GLY TYR          
SEQRES  18 B  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 B  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 B  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 B  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 B  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 B  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 C  293  MSE LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 C  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 C  293  LEU LEU PRO VAL TYR ASP LYS PRO MSE ILE TYR TYR PRO          
SEQRES   4 C  293  LEU SER THR LEU MSE LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 C  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 C  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 C  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 C  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 C  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 C  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 C  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 C  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 C  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 C  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 C  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 C  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 C  293  ARG GLY GLN LEU SER VAL GLU ILE MSE GLY ARG GLY TYR          
SEQRES  18 C  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 C  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 C  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 C  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 C  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 C  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 D  293  MSE LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 D  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 D  293  LEU LEU PRO VAL TYR ASP LYS PRO MSE ILE TYR TYR PRO          
SEQRES   4 D  293  LEU SER THR LEU MSE LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 D  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 D  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 D  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 D  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 D  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 D  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 D  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 D  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 D  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 D  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 D  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 D  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 D  293  ARG GLY GLN LEU SER VAL GLU ILE MSE GLY ARG GLY TYR          
SEQRES  18 D  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 D  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 D  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 D  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 D  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 D  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 E  293  MSE LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 E  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 E  293  LEU LEU PRO VAL TYR ASP LYS PRO MSE ILE TYR TYR PRO          
SEQRES   4 E  293  LEU SER THR LEU MSE LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 E  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 E  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 E  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 E  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 E  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 E  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 E  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 E  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 E  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 E  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 E  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 E  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 E  293  ARG GLY GLN LEU SER VAL GLU ILE MSE GLY ARG GLY TYR          
SEQRES  18 E  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 E  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 E  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 E  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 E  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 E  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 F  293  MSE LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 F  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 F  293  LEU LEU PRO VAL TYR ASP LYS PRO MSE ILE TYR TYR PRO          
SEQRES   4 F  293  LEU SER THR LEU MSE LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 F  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 F  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 F  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 F  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 F  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 F  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 F  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 F  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 F  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 F  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 F  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 F  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 F  293  ARG GLY GLN LEU SER VAL GLU ILE MSE GLY ARG GLY TYR          
SEQRES  18 F  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 F  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 F  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 F  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 F  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 F  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 G  293  MSE LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 G  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 G  293  LEU LEU PRO VAL TYR ASP LYS PRO MSE ILE TYR TYR PRO          
SEQRES   4 G  293  LEU SER THR LEU MSE LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 G  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 G  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 G  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 G  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 G  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 G  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 G  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 G  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 G  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 G  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 G  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 G  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 G  293  ARG GLY GLN LEU SER VAL GLU ILE MSE GLY ARG GLY TYR          
SEQRES  18 G  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 G  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 G  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 G  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 G  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 G  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 H  293  MSE LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 H  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 H  293  LEU LEU PRO VAL TYR ASP LYS PRO MSE ILE TYR TYR PRO          
SEQRES   4 H  293  LEU SER THR LEU MSE LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 H  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 H  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 H  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 H  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 H  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 H  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 H  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 H  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 H  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 H  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 H  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 H  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 H  293  ARG GLY GLN LEU SER VAL GLU ILE MSE GLY ARG GLY TYR          
SEQRES  18 H  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 H  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 H  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 H  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 H  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 H  293  LEU LEU THR GLU THR VAL TYR                                  
MODRES 1G23 MSE A   35  MET  SELENOMETHIONINE                                   
MODRES 1G23 MSE A   44  MET  SELENOMETHIONINE                                   
MODRES 1G23 MSE A  217  MET  SELENOMETHIONINE                                   
MODRES 1G23 MSE B   35  MET  SELENOMETHIONINE                                   
MODRES 1G23 MSE B   44  MET  SELENOMETHIONINE                                   
MODRES 1G23 MSE B  217  MET  SELENOMETHIONINE                                   
MODRES 1G23 MSE C   35  MET  SELENOMETHIONINE                                   
MODRES 1G23 MSE C   44  MET  SELENOMETHIONINE                                   
MODRES 1G23 MSE C  217  MET  SELENOMETHIONINE                                   
MODRES 1G23 MSE D   35  MET  SELENOMETHIONINE                                   
MODRES 1G23 MSE D   44  MET  SELENOMETHIONINE                                   
MODRES 1G23 MSE D  217  MET  SELENOMETHIONINE                                   
MODRES 1G23 MSE E   35  MET  SELENOMETHIONINE                                   
MODRES 1G23 MSE E   44  MET  SELENOMETHIONINE                                   
MODRES 1G23 MSE E  217  MET  SELENOMETHIONINE                                   
MODRES 1G23 MSE F   35  MET  SELENOMETHIONINE                                   
MODRES 1G23 MSE F   44  MET  SELENOMETHIONINE                                   
MODRES 1G23 MSE F  217  MET  SELENOMETHIONINE                                   
MODRES 1G23 MSE G   35  MET  SELENOMETHIONINE                                   
MODRES 1G23 MSE G   44  MET  SELENOMETHIONINE                                   
MODRES 1G23 MSE G  217  MET  SELENOMETHIONINE                                   
MODRES 1G23 MSE H   35  MET  SELENOMETHIONINE                                   
MODRES 1G23 MSE H   44  MET  SELENOMETHIONINE                                   
MODRES 1G23 MSE H  217  MET  SELENOMETHIONINE                                   
HET    MSE  A  35       8                                                       
HET    MSE  A  44       8                                                       
HET    MSE  A 217       8                                                       
HET    MSE  B  35       8                                                       
HET    MSE  B  44       8                                                       
HET    MSE  B 217       8                                                       
HET    MSE  C  35       8                                                       
HET    MSE  C  44       8                                                       
HET    MSE  C 217       8                                                       
HET    MSE  D  35       8                                                       
HET    MSE  D  44       8                                                       
HET    MSE  D 217       8                                                       
HET    MSE  E  35       8                                                       
HET    MSE  E  44       8                                                       
HET    MSE  E 217       8                                                       
HET    MSE  F  35       8                                                       
HET    MSE  F  44       8                                                       
HET    MSE  F 217       8                                                       
HET    MSE  G  35       8                                                       
HET    MSE  G  44       8                                                       
HET    MSE  G 217       8                                                       
HET    MSE  H  35       8                                                       
HET    MSE  H  44       8                                                       
HET    MSE  H 217       8                                                       
HET    G1P  A 500      16                                                       
HET    SO4  A 600       5                                                       
HET    G1P  B 501      16                                                       
HET    SO4  B 601       5                                                       
HET    G1P  C 502      16                                                       
HET    SO4  C 602       5                                                       
HET    G1P  D 503      16                                                       
HET    SO4  D 603       5                                                       
HET    SO4  D 608       5                                                       
HET    G1P  E 504      16                                                       
HET    SO4  E 604       5                                                       
HET    SO4  E 609       5                                                       
HET    G1P  F 505      16                                                       
HET    SO4  F 605       5                                                       
HET    SO4  F 610       5                                                       
HET    SO4  F 611       5                                                       
HET    G1P  G 506      16                                                       
HET    SO4  G 606       5                                                       
HET    SO4  G 612       5                                                       
HET    G1P  H 507      16                                                       
HET    SO4  H 607       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     G1P 1-O-PHOSPHONO-ALPHA-D-GLUCOPYRANOSE                              
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  MSE    24(C5 H11 N O2 SE)                                           
FORMUL   9  G1P    8(C6 H13 O9 P)                                               
FORMUL  10  SO4    13(O4 S 2-)                                                  
HELIX    1   1 GLY A   13  HIS A   17  5                                   5    
HELIX    2   2 PRO A   18  ALA A   22  5                                   5    
HELIX    3   3 SER A   24  LEU A   27  5                                   4    
HELIX    4   4 ILE A   36  ALA A   46  1                                  11    
HELIX    5   5 ASP A   59  GLY A   68  1                                  10    
HELIX    6   6 GLY A   70  GLY A   74  5                                   5    
HELIX    7   7 ALA A   89  GLY A   95  1                                   7    
HELIX    8   8 GLY A   95  GLY A  100  1                                   6    
HELIX    9   9 ASP A  117  GLN A  127  1                                  11    
HELIX   10  10 ASP A  141  ARG A  144  5                                   4    
HELIX   11  11 GLN A  181  ASP A  188  1                                   8    
HELIX   12  12 GLU A  198  ARG A  209  1                                  12    
HELIX   13  13 THR A  228  GLY A  247  1                                  20    
HELIX   14  14 CYS A  252  GLN A  260  1                                   9    
HELIX   15  15 ASP A  264  ALA A  273  1                                  10    
HELIX   16  16 PRO A  274  ALA A  276  5                                   3    
HELIX   17  17 ASN A  278  LEU A  287  1                                  10    
HELIX   18  18 LEU A  288  GLU A  290  5                                   3    
HELIX   19  19 GLY B   13  HIS B   17  5                                   5    
HELIX   20  20 SER B   24  LEU B   27  5                                   4    
HELIX   21  21 ILE B   36  ALA B   46  1                                  11    
HELIX   22  22 ASP B   59  GLY B   68  1                                  10    
HELIX   23  23 GLY B   70  GLY B   74  5                                   5    
HELIX   24  24 ALA B   89  GLY B   95  1                                   7    
HELIX   25  25 GLY B   95  GLY B  100  1                                   6    
HELIX   26  26 ASP B  117  ARG B  128  1                                  12    
HELIX   27  27 ASP B  141  ARG B  144  5                                   4    
HELIX   28  28 GLN B  181  ASP B  188  1                                   8    
HELIX   29  29 GLU B  198  ARG B  209  1                                  12    
HELIX   30  30 THR B  228  GLY B  247  1                                  20    
HELIX   31  31 CYS B  252  GLN B  260  1                                   9    
HELIX   32  32 ASP B  264  ALA B  273  1                                  10    
HELIX   33  33 PRO B  274  ALA B  276  5                                   3    
HELIX   34  34 ASN B  278  LEU B  287  1                                  10    
HELIX   35  35 LEU B  288  GLU B  290  5                                   3    
HELIX   36  36 PRO C   18  ALA C   22  5                                   5    
HELIX   37  37 SER C   24  LEU C   27  5                                   4    
HELIX   38  38 ILE C   36  ALA C   46  1                                  11    
HELIX   39  39 ASP C   59  GLY C   68  1                                  10    
HELIX   40  40 GLY C   70  GLY C   74  5                                   5    
HELIX   41  41 ALA C   89  GLY C   95  1                                   7    
HELIX   42  42 GLY C   95  GLY C  100  1                                   6    
HELIX   43  43 ASP C  117  GLN C  127  1                                  11    
HELIX   44  44 ASP C  141  ARG C  144  5                                   4    
HELIX   45  45 GLN C  181  ASP C  188  1                                   8    
HELIX   46  46 GLU C  198  ARG C  209  1                                  12    
HELIX   47  47 THR C  228  GLY C  247  1                                  20    
HELIX   48  48 CYS C  252  GLN C  260  1                                   9    
HELIX   49  49 ASP C  264  ALA C  273  1                                  10    
HELIX   50  50 PRO C  274  ALA C  276  5                                   3    
HELIX   51  51 ASN C  278  LEU C  287  1                                  10    
HELIX   52  52 LEU C  288  GLU C  290  5                                   3    
HELIX   53  53 PRO D   18  ALA D   22  5                                   5    
HELIX   54  54 SER D   24  LEU D   27  5                                   4    
HELIX   55  55 ILE D   36  ALA D   46  1                                  11    
HELIX   56  56 ASP D   59  GLY D   68  1                                  10    
HELIX   57  57 GLY D   70  GLY D   74  5                                   5    
HELIX   58  58 GLY D   87  ALA D   89  5                                   3    
HELIX   59  59 GLN D   90  GLY D   95  1                                   6    
HELIX   60  60 GLY D   95  GLY D  100  1                                   6    
HELIX   61  61 ASP D  117  GLN D  127  1                                  11    
HELIX   62  62 ASP D  141  ARG D  144  5                                   4    
HELIX   63  63 GLN D  181  ASP D  188  1                                   8    
HELIX   64  64 GLU D  198  ARG D  209  1                                  12    
HELIX   65  65 THR D  228  GLY D  247  1                                  20    
HELIX   66  66 CYS D  252  GLN D  260  1                                   9    
HELIX   67  67 ASP D  264  ALA D  273  1                                  10    
HELIX   68  68 PRO D  274  ALA D  276  5                                   3    
HELIX   69  69 ASN D  278  LEU D  288  1                                  11    
HELIX   70  70 GLY E   13  HIS E   17  5                                   5    
HELIX   71  71 PRO E   18  ALA E   22  5                                   5    
HELIX   72  72 SER E   24  LEU E   27  5                                   4    
HELIX   73  73 ILE E   36  ALA E   46  1                                  11    
HELIX   74  74 ASP E   59  GLY E   68  1                                  10    
HELIX   75  75 GLY E   70  GLY E   74  5                                   5    
HELIX   76  76 ALA E   89  GLY E   95  1                                   7    
HELIX   77  77 GLY E   95  GLY E  100  1                                   6    
HELIX   78  78 ASP E  117  GLN E  127  1                                  11    
HELIX   79  79 ASP E  141  ARG E  144  5                                   4    
HELIX   80  80 GLN E  181  ASP E  188  1                                   8    
HELIX   81  81 GLU E  198  ARG E  209  1                                  12    
HELIX   82  82 THR E  228  GLY E  247  1                                  20    
HELIX   83  83 CYS E  252  GLN E  260  1                                   9    
HELIX   84  84 ASP E  264  ALA E  273  1                                  10    
HELIX   85  85 PRO E  274  ALA E  276  5                                   3    
HELIX   86  86 ASN E  278  LEU E  287  1                                  10    
HELIX   87  87 GLY F   13  HIS F   17  5                                   5    
HELIX   88  88 PRO F   18  ALA F   22  5                                   5    
HELIX   89  89 SER F   24  LEU F   27  5                                   4    
HELIX   90  90 ILE F   36  ALA F   46  1                                  11    
HELIX   91  91 ASP F   59  GLY F   68  1                                  10    
HELIX   92  92 GLY F   70  GLY F   74  5                                   5    
HELIX   93  93 ALA F   89  GLY F   95  1                                   7    
HELIX   94  94 GLY F   95  GLY F  100  1                                   6    
HELIX   95  95 ASP F  117  GLN F  127  1                                  11    
HELIX   96  96 ASP F  141  ARG F  144  5                                   4    
HELIX   97  97 GLN F  181  ASP F  188  1                                   8    
HELIX   98  98 GLU F  198  ARG F  209  1                                  12    
HELIX   99  99 THR F  228  GLY F  247  1                                  20    
HELIX  100 100 CYS F  252  GLN F  260  1                                   9    
HELIX  101 101 ASP F  264  ALA F  273  1                                  10    
HELIX  102 102 PRO F  274  ALA F  276  5                                   3    
HELIX  103 103 ASN F  278  LEU F  287  1                                  10    
HELIX  104 104 LEU F  288  GLU F  290  5                                   3    
HELIX  105 105 SER G   24  LEU G   27  5                                   4    
HELIX  106 106 ILE G   36  ALA G   46  1                                  11    
HELIX  107 107 ASP G   59  GLY G   68  1                                  10    
HELIX  108 108 GLY G   70  GLY G   74  5                                   5    
HELIX  109 109 ALA G   89  GLY G   95  1                                   7    
HELIX  110 110 GLY G   95  GLY G  100  1                                   6    
HELIX  111 111 ASP G  117  ARG G  128  1                                  12    
HELIX  112 112 ASP G  141  ARG G  144  5                                   4    
HELIX  113 113 GLN G  181  ASP G  188  1                                   8    
HELIX  114 114 GLU G  198  ARG G  209  1                                  12    
HELIX  115 115 THR G  228  GLY G  247  1                                  20    
HELIX  116 116 CYS G  252  GLN G  260  1                                   9    
HELIX  117 117 ASP G  264  ALA G  273  1                                  10    
HELIX  118 118 PRO G  274  ALA G  276  5                                   3    
HELIX  119 119 ASN G  278  LEU G  287  1                                  10    
HELIX  120 120 LEU G  288  GLU G  290  5                                   3    
HELIX  121 121 GLY H   13  HIS H   17  5                                   5    
HELIX  122 122 SER H   24  LEU H   27  5                                   4    
HELIX  123 123 ILE H   36  ALA H   46  1                                  11    
HELIX  124 124 ASP H   59  GLY H   68  1                                  10    
HELIX  125 125 GLY H   70  GLY H   74  5                                   5    
HELIX  126 126 ALA H   89  GLY H   95  1                                   7    
HELIX  127 127 GLY H   95  GLY H  100  1                                   6    
HELIX  128 128 ASP H  117  ARG H  128  1                                  12    
HELIX  129 129 ASP H  141  ARG H  144  5                                   4    
HELIX  130 130 GLN H  181  ASP H  188  1                                   8    
HELIX  131 131 GLU H  198  ARG H  209  1                                  12    
HELIX  132 132 THR H  228  GLY H  247  1                                  20    
HELIX  133 133 CYS H  252  GLN H  260  1                                   9    
HELIX  134 134 ASP H  264  ALA H  273  1                                  10    
HELIX  135 135 PRO H  274  ALA H  276  5                                   3    
HELIX  136 136 ASN H  278  LEU H  287  1                                  10    
HELIX  137 137 LEU H  288  GLU H  290  5                                   3    
SHEET    1   A 3 LEU A 212  ILE A 216  0                                        
SHEET    2   A 3 ALA A 132  HIS A 138  1  O  ALA A 132   N  SER A 213           
SHEET    3   A 3 TYR A 170  VAL A 172 -1  O  ALA A 171   N  TYR A 137           
SHEET    1   B 7 LEU A 212  ILE A 216  0                                        
SHEET    2   B 7 ALA A 132  HIS A 138  1  O  ALA A 132   N  SER A 213           
SHEET    3   B 7 LEU A 175  TYR A 178 -1  N  PHE A 177   O  SER A 133           
SHEET    4   B 7 LEU A 103  LEU A 108 -1  N  SER A 104   O  TYR A 178           
SHEET    5   B 7 ARG A   3  LEU A   8  1  N  LYS A   4   O  LEU A 103           
SHEET    6   B 7 GLU A  50  SER A  55  1  O  GLU A  50   N  GLY A   5           
SHEET    7   B 7 ASP A  76  VAL A  81  1  O  ASP A  76   N  ILE A  51           
SHEET    1   C 2 PRO A  29  VAL A  30  0                                        
SHEET    2   C 2 LYS A  33  PRO A  34 -1  O  LYS A  33   N  VAL A  30           
SHEET    1   D 2 ASN A 111  TYR A 114  0                                        
SHEET    2   D 2 ALA A 222  ASP A 225 -1  N  ALA A 222   O  TYR A 114           
SHEET    1   E 2 GLY A 146  PHE A 150  0                                        
SHEET    2   E 2 ALA A 156  GLU A 161 -1  N  ILE A 157   O  GLU A 149           
SHEET    1   F 7 ASP B  76  VAL B  81  0                                        
SHEET    2   F 7 GLU B  50  SER B  55  1  O  ILE B  51   N  GLN B  78           
SHEET    3   F 7 ARG B   3  LEU B   8  1  O  GLY B   5   N  LEU B  52           
SHEET    4   F 7 LEU B 103  LEU B 108  1  O  LEU B 103   N  LYS B   4           
SHEET    5   F 7 TYR B 170  TYR B 178 -1  O  GLY B 174   N  LEU B 108           
SHEET    6   F 7 ALA B 132  HIS B 138 -1  O  SER B 133   N  PHE B 177           
SHEET    7   F 7 LEU B 212  ILE B 216  1  N  SER B 213   O  ALA B 132           
SHEET    1   G 2 PRO B  29  VAL B  30  0                                        
SHEET    2   G 2 LYS B  33  PRO B  34 -1  O  LYS B  33   N  VAL B  30           
SHEET    1   H 2 ASN B 111  TYR B 114  0                                        
SHEET    2   H 2 ALA B 222  ASP B 225 -1  O  ALA B 222   N  TYR B 114           
SHEET    1   I 2 GLY B 146  PHE B 150  0                                        
SHEET    2   I 2 ALA B 156  GLU B 161 -1  N  ILE B 157   O  GLU B 149           
SHEET    1   J 5 ASP C  76  VAL C  81  0                                        
SHEET    2   J 5 GLU C  50  SER C  55  1  O  ILE C  51   N  GLN C  78           
SHEET    3   J 5 ARG C   3  LEU C   8  1  O  GLY C   5   N  LEU C  52           
SHEET    4   J 5 LEU C 103  LEU C 108  1  O  LEU C 103   N  LYS C   4           
SHEET    5   J 5 LEU C 175  TYR C 178 -1  N  TYR C 176   O  LEU C 106           
SHEET    1   K 2 PRO C  29  VAL C  30  0                                        
SHEET    2   K 2 LYS C  33  PRO C  34 -1  O  LYS C  33   N  VAL C  30           
SHEET    1   L 2 ASN C 111  TYR C 114  0                                        
SHEET    2   L 2 ALA C 222  ASP C 225 -1  N  ALA C 222   O  TYR C 114           
SHEET    1   M 3 TYR C 170  VAL C 172  0                                        
SHEET    2   M 3 ALA C 132  HIS C 138 -1  N  TYR C 137   O  ALA C 171           
SHEET    3   M 3 LEU C 212  ILE C 216  1  O  SER C 213   N  VAL C 134           
SHEET    1   N 2 GLY C 146  PHE C 150  0                                        
SHEET    2   N 2 ALA C 156  GLU C 161 -1  N  ILE C 157   O  GLU C 149           
SHEET    1   O 5 ASP D  76  VAL D  81  0                                        
SHEET    2   O 5 GLU D  50  SER D  55  1  N  ILE D  51   O  ASP D  76           
SHEET    3   O 5 ARG D   3  LEU D   8  1  O  GLY D   5   N  LEU D  52           
SHEET    4   O 5 LEU D 103  LEU D 108  1  O  LEU D 103   N  LYS D   4           
SHEET    5   O 5 LEU D 175  TYR D 178 -1  N  TYR D 176   O  LEU D 106           
SHEET    1   P 2 PRO D  29  VAL D  30  0                                        
SHEET    2   P 2 LYS D  33  PRO D  34 -1  O  LYS D  33   N  VAL D  30           
SHEET    1   Q 2 ASN D 111  TYR D 114  0                                        
SHEET    2   Q 2 ALA D 222  ASP D 225 -1  N  ALA D 222   O  TYR D 114           
SHEET    1   R 3 TYR D 170  VAL D 172  0                                        
SHEET    2   R 3 ALA D 132  HIS D 138 -1  N  TYR D 137   O  ALA D 171           
SHEET    3   R 3 LEU D 212  ILE D 216  1  N  SER D 213   O  ALA D 132           
SHEET    1   S 2 GLY D 146  PHE D 150  0                                        
SHEET    2   S 2 ALA D 156  GLU D 161 -1  N  ILE D 157   O  GLU D 149           
SHEET    1   T 3 LEU E 212  ILE E 216  0                                        
SHEET    2   T 3 ALA E 132  HIS E 138  1  O  ALA E 132   N  SER E 213           
SHEET    3   T 3 TYR E 170  VAL E 172 -1  O  ALA E 171   N  TYR E 137           
SHEET    1   U 7 LEU E 212  ILE E 216  0                                        
SHEET    2   U 7 ALA E 132  HIS E 138  1  O  ALA E 132   N  SER E 213           
SHEET    3   U 7 LEU E 175  TYR E 178 -1  N  PHE E 177   O  SER E 133           
SHEET    4   U 7 LEU E 103  LEU E 108 -1  N  SER E 104   O  TYR E 178           
SHEET    5   U 7 ARG E   3  LEU E   8  1  N  LYS E   4   O  LEU E 103           
SHEET    6   U 7 GLU E  50  SER E  55  1  O  GLU E  50   N  GLY E   5           
SHEET    7   U 7 ASP E  76  VAL E  81  1  O  ASP E  76   N  ILE E  51           
SHEET    1   V 2 PRO E  29  VAL E  30  0                                        
SHEET    2   V 2 LYS E  33  PRO E  34 -1  O  LYS E  33   N  VAL E  30           
SHEET    1   W 2 ASN E 111  TYR E 114  0                                        
SHEET    2   W 2 ALA E 222  ASP E 225 -1  N  ALA E 222   O  TYR E 114           
SHEET    1   X 2 GLY E 146  PHE E 150  0                                        
SHEET    2   X 2 ALA E 156  GLU E 161 -1  N  ILE E 157   O  GLU E 149           
SHEET    1   Y 3 LEU F 212  ILE F 216  0                                        
SHEET    2   Y 3 ALA F 132  HIS F 138  1  O  ALA F 132   N  SER F 213           
SHEET    3   Y 3 TYR F 170  VAL F 172 -1  O  ALA F 171   N  TYR F 137           
SHEET    1   Z 7 LEU F 212  ILE F 216  0                                        
SHEET    2   Z 7 ALA F 132  HIS F 138  1  O  ALA F 132   N  SER F 213           
SHEET    3   Z 7 LEU F 175  TYR F 178 -1  N  PHE F 177   O  SER F 133           
SHEET    4   Z 7 LEU F 103  LEU F 108 -1  N  SER F 104   O  TYR F 178           
SHEET    5   Z 7 ARG F   3  LEU F   8  1  N  LYS F   4   O  LEU F 103           
SHEET    6   Z 7 GLU F  50  SER F  55  1  O  GLU F  50   N  GLY F   5           
SHEET    7   Z 7 ASP F  76  VAL F  81  1  O  ASP F  76   N  ILE F  51           
SHEET    1  AA 2 PRO F  29  VAL F  30  0                                        
SHEET    2  AA 2 LYS F  33  PRO F  34 -1  O  LYS F  33   N  VAL F  30           
SHEET    1  AB 2 ASN F 111  TYR F 114  0                                        
SHEET    2  AB 2 ALA F 222  ASP F 225 -1  N  ALA F 222   O  TYR F 114           
SHEET    1  AC 2 GLY F 146  PHE F 150  0                                        
SHEET    2  AC 2 ALA F 156  GLU F 161 -1  N  ILE F 157   O  GLU F 149           
SHEET    1  AD 3 LEU G 212  ILE G 216  0                                        
SHEET    2  AD 3 ALA G 132  HIS G 138  1  O  ALA G 132   N  SER G 213           
SHEET    3  AD 3 TYR G 170  VAL G 172 -1  O  ALA G 171   N  TYR G 137           
SHEET    1  AE 7 LEU G 212  ILE G 216  0                                        
SHEET    2  AE 7 ALA G 132  HIS G 138  1  O  ALA G 132   N  SER G 213           
SHEET    3  AE 7 LEU G 175  TYR G 178 -1  N  PHE G 177   O  SER G 133           
SHEET    4  AE 7 LEU G 103  LEU G 108 -1  N  SER G 104   O  TYR G 178           
SHEET    5  AE 7 ARG G   3  LEU G   8  1  N  LYS G   4   O  LEU G 103           
SHEET    6  AE 7 GLU G  50  SER G  55  1  O  GLU G  50   N  GLY G   5           
SHEET    7  AE 7 ASP G  76  VAL G  81  1  O  ASP G  76   N  ILE G  51           
SHEET    1  AF 2 PRO G  29  VAL G  30  0                                        
SHEET    2  AF 2 LYS G  33  PRO G  34 -1  O  LYS G  33   N  VAL G  30           
SHEET    1  AG 2 ASN G 111  TYR G 114  0                                        
SHEET    2  AG 2 ALA G 222  ASP G 225 -1  N  ALA G 222   O  TYR G 114           
SHEET    1  AH 2 GLY G 146  PHE G 150  0                                        
SHEET    2  AH 2 ALA G 156  GLU G 161 -1  N  ILE G 157   O  GLU G 149           
SHEET    1  AI 7 ASP H  76  VAL H  81  0                                        
SHEET    2  AI 7 GLU H  50  SER H  55  1  O  ILE H  51   N  GLN H  78           
SHEET    3  AI 7 ARG H   3  LEU H   8  1  O  GLY H   5   N  LEU H  52           
SHEET    4  AI 7 LEU H 103  LEU H 108  1  O  LEU H 103   N  LYS H   4           
SHEET    5  AI 7 TYR H 170  TYR H 178 -1  O  GLY H 174   N  LEU H 108           
SHEET    6  AI 7 ALA H 132  HIS H 138 -1  O  SER H 133   N  PHE H 177           
SHEET    7  AI 7 LEU H 212  ILE H 216  1  N  SER H 213   O  ALA H 132           
SHEET    1  AJ 2 PRO H  29  VAL H  30  0                                        
SHEET    2  AJ 2 LYS H  33  PRO H  34 -1  O  LYS H  33   N  VAL H  30           
SHEET    1  AK 2 ASN H 111  TYR H 114  0                                        
SHEET    2  AK 2 ALA H 222  ASP H 225 -1  N  ALA H 222   O  TYR H 114           
SHEET    1  AL 2 GLY H 146  PHE H 150  0                                        
SHEET    2  AL 2 ALA H 156  GLU H 161 -1  N  ILE H 157   O  GLU H 149           
LINK         C   PRO A  34                 N   MSE A  35     1555   1555  1.32  
LINK         C   MSE A  35                 N   ILE A  36     1555   1555  1.31  
LINK         C   LEU A  43                 N   MSE A  44     1555   1555  1.32  
LINK         C   MSE A  44                 N   LEU A  45     1555   1555  1.32  
LINK         C   ILE A 216                 N   MSE A 217     1555   1555  1.33  
LINK         C   MSE A 217                 N   GLY A 218     1555   1555  1.32  
LINK         C   PRO B  34                 N   MSE B  35     1555   1555  1.33  
LINK         C   MSE B  35                 N   ILE B  36     1555   1555  1.31  
LINK         C   LEU B  43                 N   MSE B  44     1555   1555  1.33  
LINK         C   MSE B  44                 N   LEU B  45     1555   1555  1.32  
LINK         C   ILE B 216                 N   MSE B 217     1555   1555  1.33  
LINK         C   MSE B 217                 N   GLY B 218     1555   1555  1.31  
LINK         C   PRO C  34                 N   MSE C  35     1555   1555  1.34  
LINK         C   MSE C  35                 N   ILE C  36     1555   1555  1.32  
LINK         C   LEU C  43                 N   MSE C  44     1555   1555  1.32  
LINK         C   MSE C  44                 N   LEU C  45     1555   1555  1.32  
LINK         C   ILE C 216                 N   MSE C 217     1555   1555  1.32  
LINK         C   MSE C 217                 N   GLY C 218     1555   1555  1.32  
LINK         C   PRO D  34                 N   MSE D  35     1555   1555  1.34  
LINK         C   MSE D  35                 N   ILE D  36     1555   1555  1.32  
LINK         C   LEU D  43                 N   MSE D  44     1555   1555  1.34  
LINK         C   MSE D  44                 N   LEU D  45     1555   1555  1.32  
LINK         C   ILE D 216                 N   MSE D 217     1555   1555  1.33  
LINK         C   MSE D 217                 N   GLY D 218     1555   1555  1.32  
LINK         C   PRO E  34                 N   MSE E  35     1555   1555  1.33  
LINK         C   MSE E  35                 N   ILE E  36     1555   1555  1.32  
LINK         C   LEU E  43                 N   MSE E  44     1555   1555  1.33  
LINK         C   MSE E  44                 N   LEU E  45     1555   1555  1.32  
LINK         C   ILE E 216                 N   MSE E 217     1555   1555  1.32  
LINK         C   MSE E 217                 N   GLY E 218     1555   1555  1.32  
LINK         C   PRO F  34                 N   MSE F  35     1555   1555  1.33  
LINK         C   MSE F  35                 N   ILE F  36     1555   1555  1.31  
LINK         C   LEU F  43                 N   MSE F  44     1555   1555  1.33  
LINK         C   MSE F  44                 N   LEU F  45     1555   1555  1.32  
LINK         C   ILE F 216                 N   MSE F 217     1555   1555  1.32  
LINK         C   MSE F 217                 N   GLY F 218     1555   1555  1.33  
LINK         C   PRO G  34                 N   MSE G  35     1555   1555  1.33  
LINK         C   MSE G  35                 N   ILE G  36     1555   1555  1.32  
LINK         C   LEU G  43                 N   MSE G  44     1555   1555  1.32  
LINK         C   MSE G  44                 N   LEU G  45     1555   1555  1.33  
LINK         C   ILE G 216                 N   MSE G 217     1555   1555  1.33  
LINK         C   MSE G 217                 N   GLY G 218     1555   1555  1.33  
LINK         C   PRO H  34                 N   MSE H  35     1555   1555  1.31  
LINK         C   MSE H  35                 N   ILE H  36     1555   1555  1.32  
LINK         C   LEU H  43                 N   MSE H  44     1555   1555  1.33  
LINK         C   MSE H  44                 N   LEU H  45     1555   1555  1.32  
LINK         C   ILE H 216                 N   MSE H 217     1555   1555  1.33  
LINK         C   MSE H 217                 N   GLY H 218     1555   1555  1.32  
CISPEP   1 HIS A   17    PRO A   18          0         2.39                     
CISPEP   2 HIS B   17    PRO B   18          0         2.59                     
CISPEP   3 HIS C   17    PRO C   18          0        -7.99                     
CISPEP   4 HIS D   17    PRO D   18          0        -2.88                     
CISPEP   5 HIS E   17    PRO E   18          0       -12.95                     
CISPEP   6 HIS F   17    PRO F   18          0       -12.72                     
CISPEP   7 HIS G   17    PRO G   18          0         1.43                     
CISPEP   8 HIS H   17    PRO H   18          0         1.36                     
CRYST1   71.583   73.901  133.748  89.81  80.31  80.18 P 1           8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013970 -0.002419 -0.002449        0.00000                         
SCALE2      0.000000  0.013733  0.000358        0.00000                         
SCALE3      0.000000  0.000000  0.007587        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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